ID   NAGZ_VIBCM              Reviewed;         330 AA.
AC   C3LSU7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   02-SEP-2026, entry version 77.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000255|HAMAP-Rule:MF_00364};
DE            EC=3.2.1.52 {ECO:0000255|HAMAP-Rule:MF_00364};
DE   AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000255|HAMAP-Rule:MF_00364};
DE   AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000255|HAMAP-Rule:MF_00364};
GN   Name=nagZ {ECO:0000255|HAMAP-Rule:MF_00364};
GN   OrderedLocusNames=VCM66_0650;
OS   Vibrio cholerae serotype O1 (strain M66-2).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=579112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M66-2;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
CC   -!- FUNCTION: Plays a role in peptidoglycan recycling by cleaving the
CC       terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-
CC       linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-
CC       acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
CC       {ECO:0000255|HAMAP-Rule:MF_00364}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC         residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00364};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC       {ECO:0000255|HAMAP-Rule:MF_00364}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00364}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00364}.
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DR   EMBL; CP001233; ACP04973.1; -; Genomic_DNA.
DR   RefSeq; WP_000529115.1; NC_012578.1.
DR   AlphaFoldDB; C3LSU7; -.
DR   SMR; C3LSU7; -.
DR   KEGG; vcm:VCM66_0650; -.
DR   HOGENOM; CLU_008392_0_0_6; -.
DR   UniPathway; UPA00544; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule.
DR   FunFam; 3.20.20.300:FF:000001; Beta-hexosaminidase; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   HAMAP; MF_00364; NagZ; 1.
DR   InterPro; IPR022956; Beta_hexosaminidase_bac.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR050226; NagZ_Beta-hexosaminidase.
DR   NCBIfam; NF003740; PRK05337.1; 1.
DR   PANTHER; PTHR30480:SF13; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW   Cytoplasm; Glycosidase; Hydrolase; Peptidoglycan synthesis.
FT   CHAIN           1..330
FT                   /note="Beta-hexosaminidase"
FT                   /id="PRO_1000133667"
FT   ACT_SITE        173
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   ACT_SITE        242
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   BINDING         160..161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT   SITE            171
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
SQ   SEQUENCE   330 AA;  36466 MW;  A737BD82C149D3A2 CRC64;
     MGPLWLDVAG YELSAEDREI LQHPTVGGVI LFGRNYHDNQ QLLALNKAIR QAAKRPILIG
     VDQEGGRVQR FREGFSRIPP AQYYARAENG VELAEQGGWL MAAELIAHDV DLSFAPVLDM
     GFACKAIGNR AFGEDVQTVL KHSSAFLRGM KAVGMATTGK HFPGHGAVIA DSHLETPYDE
     RETIAQDMAI FRAQIEAGVL DAMMPAHVVY PHYDAQPASG SSYWLKQVLR EELGFKGIVF
     SDDLSMEGAA VMGGPVERSH QALVAGCDMI LICNKREAAV EVLDNLPIME VPQAEALLKK
     QQFSYSELKR LERWQQASAN MQRLIEQFSE
//